4K83
Crystal structure of lv-ranaspumin (Lv-RSN-1) from the foam nest of Leptodactylus vastus, orthorhombic crystal form
Summary for 4K83
| Entry DOI | 10.2210/pdb4k83/pdb |
| Related | 4K82 |
| Descriptor | Lv-ranaspumin (Lv-RSN-1) (2 entities in total) |
| Functional Keywords | alpha-helical, surfactant protein, foam nest, frog, amphibian, structural protein |
| Biological source | Leptodactylus vastus (frog) |
| Total number of polymer chains | 1 |
| Total formula weight | 23492.72 |
| Authors | Hissa, D.C.,Bezerra, G.A.,Melo, V.M.M.,Gruber, K. (deposition date: 2013-04-17, release date: 2014-03-05, Last modification date: 2024-11-27) |
| Primary citation | Cavalcante Hissa, D.,Arruda Bezerra, G.,Birner-Gruenberger, R.,Paulino Silva, L.,Uson, I.,Gruber, K.,Maciel Melo, V.M. Unique Crystal Structure of a Novel Surfactant Protein from the Foam Nest of the Frog Leptodactylus vastus. Chembiochem, 15:393-398, 2014 Cited by PubMed Abstract: Breeding by releasing eggs into stable biofoams ("foam nests") is a peculiar reproduction mode within anurans, fish, and tunicates; not much is known regarding the biochemistry or molecular mechanisms involved. Lv-ranaspumin (Lv-RSN-1) is the predominant protein from the foam nest of the frog Leptodactylus vastus. This protein shows natural surfactant activity, which is assumed to be crucial for stabilizing foam nests. We elucidated the amino acid sequence of Lv-RSN-1 by de novo sequencing with mass-spectrometry and determined the high-resolution X-ray structure of the protein. It has a unique fold mainly composed of a bundle of 11 α-helices and two small antiparallel β-strands. Lv-RSN-1 has a surface rich in hydrophilic residues and a lipophilic cavity in the region of the antiparallel β-sheet. It possesses intrinsic surface-active properties, reducing the surface tension of water from 73 to 61 mN m(-1) (15 μg mL(-1)). Lv-RSN-1 belongs to a new class of surfactants proteins for which little has been reported regarding structure or function. PubMed: 24442854DOI: 10.1002/cbic.201300726 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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